Research interests of the Department of Cell Biology encompass the basic issues of plasma membrane receptor activation and signal transduction under physiological and pathological conditions. Our activities are directed to study signalling cascades and regulation of gene expression attributed to (i) tumor pathology, (ii) immuoresponses, (iii) photosensory reaction, endocytosis and cytoskeleton reorganization. Approaches range from molecular biology to electrophysiology and whole-organism physiology. The ongoing research projects in the department are focused on:
Molecular mechanisms regulating endocytosis and exocytosis in model unicellular eukaryote Paramecium studied at the gene, protein and cellular levels; genomic and proteomic studies on the components indispensable for endosome/phagosome formation, sorting and membrane trafficking; identification of machinery involved in membrane targeting and fusion; functional analysis of the cloned Rab7 paralogous genes: real-time PCR analysis of expression on onset of endocytic internalization, pattern of cellular localization of their protein products by confocal/electron microscopic immunocytochemistry and silencing of genes; studies on Rab7 effector proteins (Prof. Elżbieta Wyroba’s laboratory).
Identification of signalling pathways regulating gene expression underlying drug-induced apoptosis of brain tumour cells and neurodegeneration; studies of molecular mechanisms underlying cytokine expression in tumour microenvironment (especially Transforming Growth factor b, FasL) and regulating tumour invasion; application of RNA interference and recombinant interfering peptide technology to study host-tumour interactions in vitro and in vivo (laboratory is a member of Polish-French GDRE); bioinformatics analysis of microarray data and genomic data bases to identify cis-regulatory gene elements associated with a particular pattern of expression (Prof. Bożena Kaminska’s laboratory).
Investigations of physiological role of phosducin and phosducin-like proteins as a regulators of G-protein transduction pathway and/or modulators of function of chaperonin CCT, during folding of cytoskeletal proteins in selected ciliates (Blepharisma, Paramecium, Stentor, Tetrahymena); electrophysiological patch-clamp investigations characterizing the structure and function of mechanosensitive ion channels in Escherichia coli membrane; the role of extracellular factors in dynamics of actin cytoskeleton in Amoeba proteus with the indentification and determination of the function of actin binding proteins (Dr. Sc. Stanisław Fabczak’s laboratory).
Studies on mechanisms of signal generation by Fcg immunoreceptors at the onset of receptor-mediated phagocytosis in macrophages and monocytes. The essential approach is to examine how the activated receptor initiates a cascade of events leading to reorganization of membrane constituents, activation of tyrosine kinases and phosphoinositide kinases. In particular, studied are: the involvement of plasma membrane rafts in Fcg receptor IIA signalling, the role of the sphingomyelin cycle and ceramide generation in the transduction of signals by the receptor, the role of PI(4,5)P2 in modulation of submembrane cytoskeleton and in internalization of membrane-associated particles (Prof. Andrzej Sobota’s laboratory).
Cytoskeleton characteristics in normal and experimentally modified morphogenesis of wild type and cells transformed by genetic engineering and morphogenetic mutants of ciliates; genomic and proteomic studies on genes essential for morphogenetic processes involving basal body duplication, cellular patterning, polarity establishment and transmission in Ciliates; genomics and functional analysis of septin genes in Paramecium and Tetrahymena; participation in European Project “Paramecium Genomics” (GDRE): functional analysis of selected developmental genes using RNA inactivation by feeding and immunocytochemical and ultrastructural analysis of basal body-related cytoskeletal structures (Prof. Maria Jerka-Dziadosz’s laboratory).
Selected publications of the Department
Koprowski P., Grajkowski W., Kubalski A. (2007) The MscS cytoplasmic domain and its conformational changes on the channel gating. Curr. Topics in Membranes, vol. 58. Mechanosensitive ion channels. Part A. Owen P. Hamill, ed., 295-309.
Sharma N., Bryant J., Włoga D., Donaldson R., Davis R.C, Jerka-Dziadosz M, Gaertig J. (2007) Katanin regulates dynamics of microtubules and biogenesis of motile cilia. J. Cell Biol.178: 1065-1079.
Śliwa M., Markovic D., Gabrusiewicz K., Synowitz M., Glass R., Zawadzka M., Wesolowska A., Kettenmann H., Kaminska B. (2007) The invasion promoting effect of microglia on glioblastoma cells is inhibited by cyclosporine A. BRAIN 130:476-489.
Wyroba E., Surmacz L., Osińska M., Wiejak J. (2007) Phagosome maturation in unicellular eukaryote Paramecium: the presence of RILP, Rab7 and LAMP-2 homologues. Eur J Histochem. 51: 163-172.
Dąbrowski M., Aerts S., Kamińska B. (2006) Prediction of a key role of motifs binding E2F and NR2F in down-regulation of numerous genes during the development of the mouse hippocampus. BMC Bioinformatics 7: 367-381.
Fabczak H., Fabczak S. (2006) Photosensory transduction in unicellular eukaryotes. A comparison between ciliate protists and photoreceptor cells of higher organisms (Invited review). J. Photochem. Photobiol.83:163-171.
Włoga D., Camba A., Rogowski K., Manning G., Jerka-Dziadosz M., Gaertig J. (2006) Members of the NIMA-related kinase family promote disassembly of cilia by multiple mechanisms. Mol. Biol. Cell 17: 2799-810.
Sobota A., Strzelecka-Kiliszek A., Gładkowska E., Yoshida Y., Mrozińska K., Kwiatkowska K. (2005) Binding of IgG-opsonized particles to FcgR is an active stage of phagocytosis that involves receptor clustering and phosphorylation.J. Immunol.175: 4450 – 4457.
Shakor Abo B. A., Kwiatkowska K., Sobota A. (2004) Cell surface ceramide generation precedes and controls FcgRII clustering and phosphorylation in rafts. J.Biol.Chem. 279: 36778-36787.
Wiejak J., Surmacz L., Wyroba E. (2004) Dynamin- and clathrin-dependent endocytic pathway in unicellular eukaryote Paramecium. Biochem. Cell Biol.82: 547-558.